EGR2_MOUSE
ID EGR2_MOUSE Reviewed; 470 AA.
AC P08152;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=E3 SUMO-protein ligase EGR2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P11161};
DE AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000305};
DE AltName: Full=Early growth response protein 2;
DE Short=EGR-2;
DE AltName: Full=Zinc finger protein Krox-20;
GN Name=Egr2; Synonyms=Egr-2, Krox-20, Zfp-25;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RX PubMed=2496302; DOI=10.1128/mcb.9.2.787-797.1989;
RA Chavrier P., Janssen-Timmen U., Mattei M.-G., Zerial M., Bravo R.,
RA Charnay P.;
RT "Structure, chromosome location, and expression of the mouse zinc finger
RT gene Krox-20: multiple gene products and coregulation with the proto-
RT oncogene c-fos.";
RL Mol. Cell. Biol. 9:787-797(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND INDUCTION.
RX PubMed=3129290; DOI=10.1002/j.1460-2075.1988.tb02780.x;
RA Chavrier P., Zerial M., Lemaire P., Almendral J., Bravo R., Charnay P.;
RT "A gene encoding a protein with zinc fingers is activated during G0/G1
RT transition in cultured cells.";
RL EMBO J. 7:29-35(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-417.
RX PubMed=2452975; DOI=10.1128/mcb.8.3.1319-1326.1988;
RA Chavrier P., Lemaire P., Revelant O., Bravo R., Charnay P.;
RT "Characterization of a mouse multigene family that encodes zinc finger
RT structures.";
RL Mol. Cell. Biol. 8:1319-1326(1988).
RN [5]
RP FUNCTION.
RX PubMed=1969796; DOI=10.1002/j.1460-2075.1990.tb08228.x;
RA Chavrier P., Vesque C., Galliot B., Vigneron M., Dolle P., Duboule D.,
RA Charnay P.;
RT "The segment-specific gene Krox-20 encodes a transcription factor with
RT binding sites in the promoter region of the Hox-1.4 gene.";
RL EMBO J. 9:1209-1218(1990).
RN [6]
RP FUNCTION.
RX PubMed=1674431; DOI=10.1016/0300-9084(91)90079-g;
RA Gilardi P., Schneider-Maunoury S., Charnay P.;
RT "Krox-20: a candidate gene for the regulation of pattern formation in the
RT hindbrain.";
RL Biochimie 73:85-91(1991).
RN [7]
RP DOMAINS.
RX PubMed=1598206; DOI=10.1093/nar/20.10.2485;
RA Vesque C., Charnay P.;
RT "Mapping functional regions of the segment-specific transcription factor
RT Krox-20.";
RL Nucleic Acids Res. 20:2485-2492(1992).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8093858; DOI=10.1016/0092-8674(93)90659-e;
RA Sham M.H., Vesque C., Nonchev S., Marshall H., Frain M., Gupta R.D.,
RA Whiting J., Wilkinson D., Charnay P., Krumlauf R.;
RT "The zinc finger gene Krox20 regulates HoxB2 (Hox2.8) during hindbrain
RT segmentation.";
RL Cell 72:183-196(1993).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=7935840; DOI=10.1038/371796a0;
RA Topilko P., Schneider-Maunoury S., Levi G., Baron-Van Evercooren A.,
RA Chennoufi A.B., Seitanidou T., Babinet C., Charnay P.;
RT "Krox-20 controls myelination in the peripheral nervous system.";
RL Nature 371:796-799(1994).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10068633; DOI=10.1242/dev.126.7.1397;
RA Zorick T.S., Syroid D.E., Brown A., Gridley T., Lemke G.;
RT "Krox-20 controls SCIP expression, cell cycle exit and susceptibility to
RT apoptosis in developing myelinating Schwann cells.";
RL Development 126:1397-1406(1999).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11509834; DOI=10.1159/000048703;
RA Turman J.E. Jr., Chopiuk N.B., Shuler C.F.;
RT "The Krox-20 null mutation differentially affects the development of
RT masticatory muscles.";
RL Dev. Neurosci. 23:113-121(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11823429; DOI=10.1093/emboj/21.3.365;
RA Manzanares M., Nardelli J., Gilardi-Hebenstreit P., Marshall H.,
RA Giudicelli F., Martinez-Pastor M.T., Krumlauf R., Charnay P.;
RT "Krox20 and kreisler co-operate in the transcriptional control of segmental
RT expression of Hoxb3 in the developing hindbrain.";
RL EMBO J. 21:365-376(2002).
RN [13]
RP FUNCTION.
RX PubMed=16054051; DOI=10.1016/j.cmet.2004.12.009;
RA Chen Z., Torrens J.I., Anand A., Spiegelman B.M., Friedman J.M.;
RT "Krox20 stimulates adipogenesis via C/EBPbeta-dependent and -independent
RT mechanisms.";
RL Cell Metab. 1:93-106(2005).
RN [14]
RP FUNCTION, INTERACTION WITH CITED1 AND SFN, MUTAGENESIS OF SER-377,
RP DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17938205; DOI=10.1128/mcb.00866-07;
RA Dillon R.L., Brown S.T., Ling C., Shioda T., Muller W.J.;
RT "An EGR2/CITED1 transcription factor complex and the 14-3-3sigma tumor
RT suppressor are involved in regulating ErbB2 expression in a transgenic-
RT mouse model of human breast cancer.";
RL Mol. Cell. Biol. 27:8648-8657(2007).
RN [15]
RP UBIQUITINATION, INTERACTION WITH WWP2, AND MUTAGENESIS OF TYR-174 AND
RP TYR-208.
RX PubMed=19651900; DOI=10.1128/mcb.00407-09;
RA Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D.;
RT "The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell
RT death by catalyzing EGR2 ubiquitination.";
RL Mol. Cell. Biol. 29:5348-5356(2009).
RN [16]
RP ACETYLATION AT LYS-247, AND MUTAGENESIS OF LYS-247.
RX PubMed=28576496; DOI=10.1016/j.bbrc.2017.05.170;
RA Noritsugu K., Ito A., Nakao Y., Yoshida M.;
RT "Identification of zinc finger transcription factor EGR2 as a novel
RT acetylated protein.";
RL Biochem. Biophys. Res. Commun. 489:455-459(2017).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ASP-408.
RX PubMed=31852952; DOI=10.1038/s41598-019-55875-4;
RA Grosz B.R., Golovchenko N.B., Ellis M., Kumar K., Nicholson G.A.,
RA Antonellis A., Kennerson M.L.;
RT "A de novo EGR2 variant, c.1232A > G p.Asp411Gly, causes severe early-onset
RT Charcot-Marie-Tooth Neuropathy Type 3 (Dejerine-Sottas Neuropathy).";
RL Sci. Rep. 9:19336-19336(2019).
CC -!- FUNCTION: Sequence-specific DNA-binding transcription factor
CC (PubMed:1969796, PubMed:1674431, PubMed:11823429, PubMed:31852952).
CC Plays a role in hindbrain segmentation by regulating the expression of
CC a subset of homeobox containing genes and in Schwann cell myelination
CC by regulating the expression of genes involved in the formation and
CC maintenance of myelin (PubMed:1969796, PubMed:1674431, PubMed:11823429,
CC PubMed:31852952, PubMed:8093858). Binds to two EGR2-consensus sites
CC EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3
CC enhancer and promotes HOXB3 transcriptional activation
CC (PubMed:11823429). Binds to specific DNA sites located in the promoter
CC region of HOXA4, HOXB2 and ERBB2 (PubMed:1969796, PubMed:8093858,
CC PubMed:17938205). Regulates hindbrain segmentation by controlling the
CC expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby
CC specifying odd and even rhombomeres (PubMed:11823429, PubMed:1674431).
CC Promotes the expression of HOXB3 in the rhombomere r5 and of HOXB3 in
CC r3 and r5 in the hindbrain (PubMed:11823429, PubMed:8093858). Regulates
CC myelination in the peripheral nervous system after birth, possibly by
CC regulating the expression of myelin proteins, such as MPZ, and by
CC promoting the differentiation of Schwann cells (PubMed:7935840,
CC PubMed:10068633). Involved in the development of the jaw openener
CC musculature, probably by playing a role in its innervation through
CC trigeminal motor neurons (PubMed:11509834). May play a role in
CC adipogenesis, possibly by regulating the expression of CEBPB
CC (PubMed:16054051). {ECO:0000269|PubMed:10068633,
CC ECO:0000269|PubMed:11509834, ECO:0000269|PubMed:11823429,
CC ECO:0000269|PubMed:16054051, ECO:0000269|PubMed:1674431,
CC ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:1969796,
CC ECO:0000269|PubMed:31852952, ECO:0000269|PubMed:7935840,
CC ECO:0000269|PubMed:8093858}.
CC -!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
CC coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
CC transcriptional activity. {ECO:0000250|UniProtKB:P11161}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with WWP2
CC (PubMed:19651900). Interacts with UBC9 (By similarity). Interacts with
CC CITED1 (PubMed:17938205). Interacts (via phosphorylated form) with SFN
CC (PubMed:17938205). {ECO:0000250|UniProtKB:P11161,
CC ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:19651900}.
CC -!- INTERACTION:
CC P08152; Q8C5D8-1: Pias2; NbExp=5; IntAct=EBI-7070449, EBI-8064899;
CC P08152; P63280: Ube2i; NbExp=2; IntAct=EBI-7070449, EBI-80180;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938205}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P08152-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P08152-2; Sequence=VSP_006864;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the thymus.
CC {ECO:0000269|PubMed:17938205}.
CC -!- DEVELOPMENTAL STAGE: Before 8 dpc, expressed in the future rhombomere
CC r3 at 0-3 somites, followed by expression in rhombomere r5 in 4-7
CC somites at 8 dpc, and maintained until 12 somites (PubMed:8093858).
CC Expressed in migrating neural crest cells from r5/r6 (PubMed:8093858).
CC Expressed in boundary cap cells that surround nerve exit points from
CC the central nervous system at 10.5 dpc (PubMed:7935840,
CC PubMed:8093858). Up to 14.5 dpc, expressed in motor and sensory roots
CC of cranial and spinal nerves (PubMed:7935840). After 15.5 dpc,
CC expressed in the entire peripheral nervous system (PubMed:7935840).
CC Expressed in the embryonic nervous system (PubMed:17938205). Expressed
CC in myelinating Schwann cells 2 weeks after birth (PubMed:7935840).
CC {ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:7935840,
CC ECO:0000269|PubMed:8093858}.
CC -!- INDUCTION: Activated during G0/G1 transition in cultured cells.
CC {ECO:0000269|PubMed:3129290}.
CC -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
CC {ECO:0000269|PubMed:19651900}.
CC -!- PTM: Acetylated at Lys-247. May be deacetylated by HDAC6, HDAC10 or
CC SIRT1. {ECO:0000269|PubMed:28576496}.
CC -!- DISRUPTION PHENOTYPE: Failure to promote expression of the Hoxb3
CC reporter in rhombomere r5 in the hindbrain (PubMed:11823429). Changed
CC morphology of the sciatic nerves, with a higher density of Schwann
CC cells, and a reduction in major components of compacted myelin,
CC including lipidic components, as well as myelin proteins Mpz and Mbp
CC (PubMed:7935840). Schwann cells in the sciatic nerves exhibit increased
CC expression of Scip, reduced expression of Mpz, elevated mitotic
CC activity and increased apoptosis at postnatal day P12
CC (PubMed:10068633). Total absence of myelin along the axons of sciatic
CC nerves at postnatal day P15 (PubMed:7935840). Does not seem to affect
CC the myelination in the central nervous system (PubMed:7935840). Signs
CC of atrophy in the jaw openener anterior digastric (AD) and mylohoid
CC (MY) muscles at 15 dpc with smaller diameter fibers, fibers with
CC triangular shape, increased amount of connective tissue surrounding the
CC fibers, suggesting a lack of neural innervation (PubMed:11509834).
CC Reduced volume of the delineated trigeminal motor nucleus and
CC restructuring of the brainstem at 15 dpc (PubMed:11509834). Reduced
CC volume in both AD and MY musculature and reduced milk indigestion after
CC birth (PubMed:11509834). {ECO:0000269|PubMed:10068633,
CC ECO:0000269|PubMed:11509834, ECO:0000269|PubMed:11823429,
CC ECO:0000269|PubMed:7935840}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; M24377; AAA39379.1; -; Genomic_DNA.
DR EMBL; M24376; AAA39379.1; JOINED; Genomic_DNA.
DR EMBL; M24377; AAA39380.1; -; Genomic_DNA.
DR EMBL; M24376; AAA39380.1; JOINED; Genomic_DNA.
DR EMBL; X06746; CAA29921.1; -; mRNA.
DR EMBL; BC009093; AAH09093.1; -; mRNA.
DR EMBL; M20759; AAA39381.1; -; Genomic_DNA.
DR CCDS; CCDS35927.2; -. [P08152-1]
DR CCDS; CCDS83706.1; -. [P08152-2]
DR PIR; A30136; A30136.
DR PIR; S00256; S00256.
DR RefSeq; NP_001334387.1; NM_001347458.1. [P08152-2]
DR RefSeq; NP_034248.2; NM_010118.3. [P08152-1]
DR RefSeq; XP_006513272.1; XM_006513209.2. [P08152-2]
DR RefSeq; XP_006513273.1; XM_006513210.2.
DR RefSeq; XP_006513274.1; XM_006513211.2.
DR RefSeq; XP_006513276.1; XM_006513213.3.
DR RefSeq; XP_011241670.1; XM_011243368.2. [P08152-2]
DR AlphaFoldDB; P08152; -.
DR SMR; P08152; -.
DR BioGRID; 199405; 7.
DR ELM; P08152; -.
DR IntAct; P08152; 5.
DR MINT; P08152; -.
DR STRING; 10090.ENSMUSP00000041053; -.
DR iPTMnet; P08152; -.
DR PhosphoSitePlus; P08152; -.
DR PaxDb; P08152; -.
DR PRIDE; P08152; -.
DR ProteomicsDB; 277805; -. [P08152-1]
DR ProteomicsDB; 277806; -. [P08152-2]
DR Antibodypedia; 14464; 516 antibodies from 43 providers.
DR DNASU; 13654; -.
DR Ensembl; ENSMUST00000048289; ENSMUSP00000041053; ENSMUSG00000037868. [P08152-1]
DR Ensembl; ENSMUST00000105438; ENSMUSP00000101078; ENSMUSG00000037868. [P08152-2]
DR GeneID; 13654; -.
DR KEGG; mmu:13654; -.
DR UCSC; uc007flx.1; mouse. [P08152-1]
DR CTD; 1959; -.
DR MGI; MGI:95296; Egr2.
DR VEuPathDB; HostDB:ENSMUSG00000037868; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158394; -.
DR InParanoid; P08152; -.
DR OMA; PQCQREL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P08152; -.
DR TreeFam; TF318980; -.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 13654; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Egr2; mouse.
DR PRO; PR:P08152; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P08152; protein.
DR Bgee; ENSMUSG00000037868; Expressed in neurectoderm and 83 other tissues.
DR ExpressionAtlas; P08152; baseline and differential.
DR Genevisible; P08152; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0035284; P:brain segmentation; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0021612; P:facial nerve structural organization; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:ARUK-UCL.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0021569; P:rhombomere 3 development; IGI:MGI.
DR GO; GO:0021660; P:rhombomere 3 formation; IMP:MGI.
DR GO; GO:0021659; P:rhombomere 3 structural organization; IDA:UniProtKB.
DR GO; GO:0021666; P:rhombomere 5 formation; IMP:MGI.
DR GO; GO:0021665; P:rhombomere 5 structural organization; IDA:UniProtKB.
DR GO; GO:0007622; P:rhythmic behavior; IDA:MGI.
DR GO; GO:0014037; P:Schwann cell differentiation; IMP:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:UniProtKB.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="E3 SUMO-protein ligase EGR2"
FT /id="PRO_0000047120"
FT ZN_FING 337..361
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 367..389
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 395..417
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 126..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:28576496"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:3129290"
FT /id="VSP_006864"
FT MUTAGEN 174
FT /note="Y->F: Abolishes interaction with WWP2; if associated
FT with F-208."
FT /evidence="ECO:0000269|PubMed:19651900"
FT MUTAGEN 208
FT /note="Y->F: Abolishes interaction with WWP2; if associated
FT with F-174."
FT /evidence="ECO:0000269|PubMed:19651900"
FT MUTAGEN 247
FT /note="K->R: Abolishes acetylation."
FT /evidence="ECO:0000269|PubMed:28576496"
FT MUTAGEN 377
FT /note="S->A: Inhibits interaction with SFN."
FT /evidence="ECO:0000269|PubMed:17938205"
FT MUTAGEN 408
FT /note="D->G: Reduces transcriptional regulatory activity."
FT /evidence="ECO:0000269|PubMed:31852952"
SQ SEQUENCE 470 AA; 49819 MW; 67712733C77960F0 CRC64;
MMTAKAVDKI PVTLSGFMHQ LPDSLYPVED LAASSVTIFP NGELGGPFDQ MNGVAGDGMI
NIDMTGEKRP LDLPYPSSFA PISAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTPPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPE LDHLYSPPPP PPPYSGCTGD
LYQDPSAFLS PPSTTSTSSL AYQPPPSYPS PKPAMDPGLI PMIPDYPGFF PSPCQRDPHG
AAGPDRKPFP CPLDSLRVPP PLTPLSTIRN FTLGGPGAGV TGPGASGGGE GPRLPGSGSA
AVTATPYNPH HLPLRPILRP RKYPNRPSKT PVHERPYPCP AEGCDRRFSR SDELTRHIRI
HTGHKPFQCR ICMRNFSRSD HLTTHIRTHT GEKPFACDYC GRKFARSDER KRHTKIHLRQ
KERKSSAPSA PPSAQSSASG PGGSQAGGSL CGNSAIGGPL ASCTSRTRTP
